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Q9JJA7 (CCNL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-L2
Alternative name(s):
Cyclin Ania-6b
Paneth cell-enhanced expression protein
Short name=PCEE
Gene names
Name:Ccnl2
Synonyms:Ania6b
ORF Names:MNCb-5160
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Also modulates the expression of critical apoptotic factor, leading to cell apoptosis By similarity.

Subunit structure

Interacts with CDK11A, CDK11B, CDK12, CDK13, SFRS2, SFRS7 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. Ref.9

Subcellular location

Nucleus speckle By similarity.

Domain

Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions By similarity.

Sequence similarities

Belongs to the cyclin family. Cyclin L subfamily.

Sequence caution

The sequence AAC52504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC52504.1 differs from that shown. Reason: Erroneous termination at position 519. Translated as stop.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionCyclin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from electronic annotation. Source: InterPro

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JJA7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JJA7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     219-224: NYMNDS → VASEGK
     225-518: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q9JJA7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     219-518: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Cyclin-L2
PRO_0000080488

Regions

Region81 – 183103Cyclin-like 1
Region196 – 28085Cyclin-like 2
Region382 – 42039RS

Amino acid modifications

Modified residue3281Phosphoserine By similarity
Modified residue3351Phosphoserine By similarity
Modified residue3451Phosphoserine By similarity
Modified residue3481Phosphoserine By similarity
Modified residue3661Phosphoserine By similarity

Natural variations

Alternative sequence219 – 518300Missing in isoform 3.
VSP_016133
Alternative sequence219 – 2246NYMNDS → VASEGK in isoform 2.
VSP_016134
Alternative sequence225 – 518294Missing in isoform 2.
VSP_016135

Experimental info

Sequence conflict161S → A in BAE41413. Ref.4
Sequence conflict161S → A in BAE33556. Ref.4
Sequence conflict161S → A in EDL15040. Ref.6
Sequence conflict161S → A in AAI32296. Ref.7
Sequence conflict1311K → R in BAC26255. Ref.4
Sequence conflict2821Y → F in AAH03773. Ref.7
Sequence conflict3171T → S in EDL15040. Ref.6
Sequence conflict3171T → S in AAH03773. Ref.7
Sequence conflict3171T → S in AAI32296. Ref.7
Sequence conflict3341E → VE in AAH03773. Ref.7
Sequence conflict3341E → VE in AAH83055. Ref.7
Sequence conflict3341E → VE in AAC52504. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C93AEE68682CDBA5

FASTA51858,005
        10         20         30         40         50         60 
MAAAAAGAAG LMAPASAACS SGSAGAAPGS QGVLIGDRLY SGVLITLENC LLPDDKLRFT 

        70         80         90        100        110        120 
PSMSSGLDVD TETGLRVVGC ELIQAAGILL RLPQVAMATG QVLFQRFFYT KSFVKHSMEH 

       130        140        150        160        170        180 
VSMACVHLAS KIEEAPRRIR DVINVFHRLR HLREKKKPVP LVLDQEYVNL KNQIIKAERR 

       190        200        210        220        230        240 
VLKELGFCVH VKHPHKIIVM YLQVLECERN QHLVQTAWNY MNDSLRTDVF VRFQPESIAC 

       250        260        270        280        290        300 
ACIYLAARTL EIPLPNRPHW FLLFGATEEE IQEICFKILQ LYTRKKVDLT HLESEVEKRK 

       310        320        330        340        350        360 
HAIEEAKARA KGLLPGTAPG LDSAAGFSPA PKLESPKEGK GGKPSPPSGK SAKRKMEGPK 

       370        380        390        400        410        420 
KAQGHSPVNG LLKGQESRSQ SRSREQSYSR SPSRSASPKR RKSDSGSTSG GSKSQSRSRS 

       430        440        450        460        470        480 
RSDSPPRQVH RGAPYKGSEV RGSRKSKDCK YLTQKPHKSR SRSSSRSRSR SRERTDNSGK 

       490        500        510 
YKKKSHYYRD QRRERSRSYE RTGHRYERDH PGHSRHRR 

« Hide

Isoform 2 [UniParc].

Checksum: 744000F7C7D3084E
Show »

FASTA22424,578
Isoform 3 [UniParc].

Checksum: 584E197FA66E601D
Show »

FASTA21824,006

References

« Hide 'large scale' references
[1]"Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an RNA polymerase II-associated cyclin."
Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M., Hyman S.E.
Neuron 32:277-287(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6.
[2]"Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[3]"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Head, Pancreas, Skin and Spleen.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Brain and Mammary gland.
[8]"Patterns of gene expression along the crypt-villus axis in mouse jejunal epithelium."
Cheng H., Bjerknes M.
Anat. Rec. 244:78-94(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 321-518.
Strain: BALB/c.
Tissue: Jejunal epithelium.
[9]"CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative splicing."
Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.
Biochem. Biophys. Res. Commun. 354:735-740(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION CDK13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF211859 mRNA. Translation: AAF23011.1.
AY337018 mRNA. Translation: AAQ01205.1.
AB041605 mRNA. Translation: BAA95088.1.
AK007552 mRNA. Translation: BAB25103.1.
AK029033 mRNA. Translation: BAC26255.1.
AK048244 mRNA. Translation: BAE43334.1.
AK156037 mRNA. Translation: BAE33556.1.
AK169857 mRNA. Translation: BAE41413.1.
AL670236 Genomic DNA. Translation: CAM18388.1.
CH466594 Genomic DNA. Translation: EDL15040.1.
BC003773 mRNA. Translation: AAH03773.2.
BC023747 mRNA. No translation available.
BC083055 mRNA. Translation: AAH83055.1.
BC132295 mRNA. Translation: AAI32296.1.
U37351 mRNA. Translation: AAC52504.1. Sequence problems.
CCDSCCDS19042.1. [Q9JJA7-1]
RefSeqNP_997561.1. NM_207678.1. [Q9JJA7-1]
UniGeneMm.23492.

3D structure databases

ProteinModelPortalQ9JJA7.
SMRQ9JJA7. Positions 50-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JJA7. 1 interaction.
MINTMINT-4129894.
STRING10090.ENSMUSP00000030944.

PTM databases

PhosphoSiteQ9JJA7.

Proteomic databases

PaxDbQ9JJA7.
PRIDEQ9JJA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030944; ENSMUSP00000030944; ENSMUSG00000029068. [Q9JJA7-1]
GeneID56036.
KEGGmmu:56036.
UCSCuc008wev.1. mouse. [Q9JJA7-3]
uc008wew.1. mouse. [Q9JJA7-1]

Organism-specific databases

CTD81669.
MGIMGI:1927119. Ccnl2.

Phylogenomic databases

eggNOGCOG5333.
GeneTreeENSGT00690000101911.
HOVERGENHBG056044.
InParanoidA2AD95.
OMADQEYVNL.
OrthoDBEOG7K9K34.
PhylomeDBQ9JJA7.
TreeFamTF101011.

Gene expression databases

BgeeQ9JJA7.
CleanExMM_CCNL2.
GenevestigatorQ9JJA7.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_C/H/T/L.
IPR017060. Cyclin_L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10026. PTHR10026. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF036580. Cyclin_L. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

ChiTaRSCCNL2. mouse.
NextBio311796.
PROQ9JJA7.
SOURCESearch...

Entry information

Entry nameCCNL2_MOUSE
AccessionPrimary (citable) accession number: Q9JJA7
Secondary accession number(s): A2AD95 expand/collapse secondary AC list , A2RSY2, Q5XK66, Q60995, Q8C136, Q8CIJ8, Q99L73, Q9QXH5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot